B1LWN4 · LIPA_METRJ
- ProteinLipoyl synthase
- GenelipA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids327 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Catalytic activity
- [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S]2+ cluster] + N6-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine + 4 H+ = [[Fe-S] cluster scaffold protein] + N6-[(R)-dihydrolipoyl]-L-lysyl-[protein] + 4 Fe3+ + 2 hydrogen sulfide + 2 5'-deoxyadenosine + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
RHEA-COMP:14568 CHEBI:33722 Position: ACHEBI:33722 Position: B+ RHEA-COMP:9928 + 2 RHEA-COMP:10000 + 2 CHEBI:59789 + 4 CHEBI:15378 = RHEA-COMP:14569 CHEBI:33722 Position: A+ RHEA-COMP:10475 + 4 CHEBI:29034 + 2 CHEBI:29919 + 2 CHEBI:17319 + 2 CHEBI:57844 + 2 RHEA-COMP:10001
Cofactor
Note: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway
Protein modification; protein lipoylation via endogenous pathway; protein N6-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 64 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 69 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 75 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 90 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 94 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 97 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 303 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | lipoate synthase activity | |
Molecular Function | metal ion binding | |
Biological Process | protein lipoylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLipoyl synthase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Methylobacteriaceae > Methylobacterium
Accessions
- Primary accessionB1LWN4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000099613 | 1-327 | Lipoyl synthase | |||
Sequence: MAVVLDTLKNDPRPVRLRHPEKAHRPDQPVQAKKPDWIRVKAPGSRAWSETQKIVREHGLVTVCEEAGCPNIGECWEKRHATFMIMGDTCTRACAFCNVRTGLPDALDLGEPDKIADSVAKLGLHHVVITSVDRDDLRDGGAEHFARTIAAIRRASPGTTVEILTPDFLRKDGALEVVVAAKPDVFNHNLETVPAKYLTVRPGARYFHSVRLLQRVKELDPAIFTKSGIMVGLGEERNEVLQLMDDLRSADVDFLTIGQYLQPSKKHHEVVRFVPPDEFKAYETTAYAKGFLLVSATPLTRSSHHAGEDFARLQAARLAKLSPALSA |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-32 | Disordered | ||||
Sequence: MAVVLDTLKNDPRPVRLRHPEKAHRPDQPVQA | ||||||
Compositional bias | 11-32 | Basic and acidic residues | ||||
Sequence: DPRPVRLRHPEKAHRPDQPVQA | ||||||
Domain | 76-292 | Radical SAM core | ||||
Sequence: WEKRHATFMIMGDTCTRACAFCNVRTGLPDALDLGEPDKIADSVAKLGLHHVVITSVDRDDLRDGGAEHFARTIAAIRRASPGTTVEILTPDFLRKDGALEVVVAAKPDVFNHNLETVPAKYLTVRPGARYFHSVRLLQRVKELDPAIFTKSGIMVGLGEERNEVLQLMDDLRSADVDFLTIGQYLQPSKKHHEVVRFVPPDEFKAYETTAYAKGFL |
Sequence similarities
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length327
- Mass (Da)36,245
- Last updated2008-04-29 v1
- ChecksumAA09B4FF34385F53
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 11-32 | Basic and acidic residues | ||||
Sequence: DPRPVRLRHPEKAHRPDQPVQA |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001001 EMBL· GenBank· DDBJ | ACB24171.1 EMBL· GenBank· DDBJ | Genomic DNA |